Cancer Diagnostics Solutions
Macrophages represent a diverse population of mononuclear phagocytes residing in tissues, originating from hematopoietic stem cells within the bone marrow. These cells perform a broad spectrum of immune functions, including non-specific phagocytosis and pinocytosis, intracellular killing of pathogens, and the processing and presentation of antigens to both T and B lymphocytes. Additionally, macrophages secrete a wide array of bioactive molecules such as lysozyme, collagenases, complement proteins, coagulation factors, prostaglandins, leukotrienes, and immunoregulatory cytokines, including interferons and interleukin-1 (IL-1).
The HAM-56 monoclonal antibody is specific for a subset of macrophages. It exhibits immunoreactivity with tingible body macrophages located in germinal centers of lymph nodes, interdigitating dendritic macrophages, and various tissue-resident macrophages, such as Kupffer cells in the liver and alveolar macrophages in the lung. In addition, HAM-56 stains a subpopulation of endothelial cells, particularly those lining capillaries and small-caliber blood vessels. While it binds to circulating monocytes, it does not exhibit cross-reactivity with B or T lymphocytes.
Mammaglobin, 10 kDa, is a cytoplasmic protein, a mammary-specific member of the uteroglobin family. It is related to a family of epithelial secretory proteins that includes prostatein and Clara cell protein.Mammaglobin occurs in about 80% of breast carcinomas.
Immunohistochemical analysis demonstrates high AMACR protein expression in prostatic adenocarcinoma, while benign prostatic epithelium typically lacks detectable expression. Furthermore, AMACR immunoreactivity is observed in premalignant prostatic lesions, including high-grade prostatic intraepithelial neoplasia (PIN) and atypical adenomatous hyperplasia, supporting its role as an early biomarker in prostate carcinogenesis.
MAP2 (Microtubule-Associated Protein 2) is expressed in two high-molecular-weight isoforms (MAP2a and MAP2b) and a low-molecular-weight variant, all derived through alternative splicing of a single gene. Its expression is developmentally regulated, reflecting its essential role in neurogenesis through the promotion of microtubule assembly. Homologous gene products in rat and mouse are neuron-specific cytoskeletal proteins localized predominantly to dendrites, where they contribute to the establishment and stabilization of dendritic architecture during neuronal differentiation. MAP2 serves as a valuable marker in the investigation of neuronal morphology in both normal and neoplastic brain tissue and is also relevant to studies of neurodegenerative disorders, including Alzheimer?s disease.
The p53 tumor suppressor gene is the most frequently mutated gene identified in human malignancies to date. Its expression exerts antiproliferative effects by inhibiting the transition of cells from the G1 to the S phase of the cell cycle. Critically, p53 mediates G1-phase arrest in response to DNA damage, thereby facilitating genomic integrity preservation.
MDM2 (murine double minute 2) was originally characterized as an oncogene in a murine transformation assay. The MDM2 protein binds directly to p53, inhibiting its transcriptional activation of downstream target genes. Amplification of the MDM2 gene occurs in a substantial proportion of human sarcomas that retain wild-type p53. In tumor cells with MDM2 overexpression, elevated p53 protein levels are tolerated without induction of growth arrest or apoptosis. These observations indicate that MDM2 overexpression constitutes a key mechanism of functional p53 inactivation during oncogenesis.
MDM2 is a nuclear phosphoprotein that binds and inhibits transactivation by tumor protein p53. It can promote tumor formation by targeting tumor suppressor proteins, such as p53, for proteasomal degradation. Overexpression of MDM2 can result in excessive inactivation of tumor protein p53, diminishing its tumor suppressor function. This protein also affects the cell cycle, apoptosis, and tumorigenesis through interactions with other proteins, including retinoblastoma 1 and ribosomal protein L5. Overexpression of MDM2 protein is detected in a variety of cancers
MDM2 is a nuclear phosphoprotein that binds and inhibits transactivation by tumor protein p53. It can promote tumor formation by targeting tumor suppressor proteins, such as p53, for proteasomal degradation. Overexpression of MDM2 can result in excessive inactivation of tumor protein p53, diminishing its tumor suppressor function. This protein also affects the cell cycle, apoptosis, and tumorigenesis through interactions with other proteins, including retinoblastoma 1 and ribosomal protein L5. Overexpression of MDM2 protein is detected in a variety of cancers
Melan-A, also known as MART-1 (Melanoma Antigen Recognized by T cells 1), is a melanocyte lineage-specific differentiation antigen that is recognized by cytotoxic T lymphocytes in patients with melanoma. It is expressed in both normal melanocytes and neoplastic cells exhibiting melanocytic differentiation. Immunohistochemical detection of MART-1 is a valuable diagnostic tool for identifying melanocytic neoplasms, particularly in the context of metastatic melanoma. Moreover, the characterization of MART-1 as a melanoma-associated antigen has significant implications for the development of targeted immunotherapeutic strategies in the management of melanoma.
MART-1 antibody (Melan-A antibody) is a mouse monoclonal antibody for immunohistochemistry from Bio SB. MART-1/Melan-A is a putative 18 kDa transmembrane protein consisting of 118 amino acids. It has a single transmembrane domain. MART-1/Melan- A is a protein antigen found on melanocytes. Antibodies against this antigen are used to recognize cells of melanocytic differentiation, useful for the diagnosis of Melanoma. The same name is used to refer to the gene which codes for this antigen. The MART-1 antibody is specific for the melanocyte lineage found in normal skin, retina, and melanocytes, but not in other normal tissues. It is thus useful as a marker for Melanocytic Tumors, with the caveat that it is normally found in benign nevi as well. This antibody is very useful in establishing the diagnosis of Metastatic Melanomas.
Metastatic melanoma is often confused with a variety of poorly differentiated carcinomas, sarcomas, and large cell lymphomas. Clone HMB45 reacts with fetal and neonatal melanocytes but not with normal adult melanocytes, and with junctional nevus cells but not with intradermal nevi, hence showing specificity for detection of melanocytic tumors. The panel of tumor markers, most commonly used in conjunction with HMB45, for evaluation of melanoma includes S-100 protein LCA, CEA, and EMA, as well as vimentin, an intermediate filament found in both melanomas and sarcomas
Mesothelioma, a form of cancer resulting from past asbestos exposure, leads to the growth of malignant cells within the mesothelium, the protective lining covering most internal organs. It is most commonly found in the pleura but can also occur in the pericardium or peritoneum. When asbestos fibers are deposited in the lung parenchyma, they can penetrate the visceral pleura and be transported to the pleural surface, where they contribute to the formation of malignant mesothelial plaques. Symptoms such as shortness of breath, cough, and chest pain due to fluid accumulation in the pleural space often do not manifest until 20 to 50 years after the initial asbestos exposure. Due to the highly aggressive nature of Mesothelioma, conventional treatments are generally ineffective, resulting in a median survival time of 6-12 months after diagnosis. Markers for Mesothelioma are valuable for studying the function and behavior of this tissue. This antibody reacts with an unidentified antigen on the microvilli of mesothelioma cells. It stains normal mesothelial cells as well as epithelial mesotheliomas, creating a thick membrane pattern due to the abundance of lung microvilli on these cells' surfaces
The mesothelin gene encodes a 69-kDa precursor protein that undergoes proteolytic cleavage to generate a 40-kDa mature form, which is tethered to the cell membrane via a glycosylphosphatidylinositol (GPI) anchor. Although the precise physiological function of mesothelin remains undefined, it has been shown to interact with MUC16 (CA125) with high affinity, a binding interaction implicated in the facilitation of peritoneal metastasis in ovarian carcinoma. Under physiological conditions, mesothelin is expressed on mesothelial cells lining the pleura, peritoneum, and pericardium. In neoplastic tissues, mesothelin is frequently overexpressed in malignant mesotheliomas and a range of epithelial malignancies, including ovarian and pancreatic adenocarcinomas, as well as cholangiocarcinomas. Owing to its tumor-restricted overexpression and cell surface localization, mesothelin has emerged as a promising target for antibody-based immunotherapeutic strategies, including immunotoxin-directed therapies in mesothelin-expressing malignancies
This monoclonal antibody (MAb) recognizes an 83kDa protein identified as MLH1. Mutations in MLH1 cause hereditary non-polyposis colorectal cancer type 2 (HNPCC2). MLH1 forms a heterodimer with PMS2 to create MutL alpha, a key component of the post-replicative DNA mismatch repair system (MMR). DNA repair begins with MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH3) binding to a DNA mismatch, followed by the recruitment of MutL alpha to the heteroduplex. The assembly of the MutL-MutS-heteroduplex complex, in the presence of RFC and PCNA, activates PMS2's endonuclease activity. This activity introduces single-strand breaks near the mismatch, creating entry points for the exonuclease EXO1 to degrade the mismatched strand. DNA methylation prevents cleavage, ensuring only the newly synthesized strand is corrected. MutL alpha (MLH1-PMS2) also interacts with DNA polymerase III's clamp loader subunits, potentially recruiting the polymerase to the MMR site. Additionally, MLH1 is involved in DNA damage signaling, which can induce cell cycle arrest and apoptosis in response to significant DNA damage. MLH1 also forms a heterodimer with MLH3 to create MutL gamma, which plays a role in meiosis
Matrix metallopeptidase 9 (MMP9), also known as gelatinase B, CLG4B, or GELB, is a member of the matrix metalloproteinase (MMP) family?zinc- and calcium-dependent endopeptidases involved in the degradation of extracellular matrix (ECM) components. MMP9 is synthesized as a 92 kDa proenzyme (zymogen) and undergoes proteolytic activation to yield an 82 kDa catalytically active form. Structurally, MMP9 comprises a gelatin-binding domain composed of three fibronectin type II repeats, a catalytic domain with a zinc-binding motif, a proline-rich segment homologous to type V collagen, and a C-terminal hemopexin-like domain.
MMP9 is produced by various cell types, including monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts, and endothelial cells. It plays critical roles in ECM remodeling, inflammation, wound repair, tumor invasion, and metastasis. In cutaneous carcinogenesis, MMP9 is derived primarily from bone marrow?origin hematopoietic cells. It preferentially degrades type IV and type V collagens.
Functional studies in rhesus macaques have implicated MMP9 in interleukin-8 (IL-8)-mediated mobilization of hematopoietic progenitor cells from bone marrow. Murine models suggest its involvement in tumor-associated stromal remodeling. Clinically, elevated MMP9 expression has been correlated with the pathogenesis and progression of idiopathic atrial fibrillation and the development of aortic aneurysms
Myeloperoxidase (MPO) is a heme-containing enzyme predominantly expressed during the differentiation of myeloid lineage cells and constitutes a major component of the azurophilic (primary) granules in neutrophils. It is initially synthesized as a single-chain precursor polypeptide, which undergoes proteolytic cleavage to yield a mature enzyme comprising two light chains and two heavy chains, forming a heterotetrameric structure. MPO catalyzes the production of reactive hypohalous acids?primarily hypochlorous acid?from hydrogen peroxide and halide ions, playing a critical role in the antimicrobial defense mechanisms of neutrophils. Pathological conditions associated with MPO include Myeloperoxidase Deficiency and Familial Alzheimer's Disease Type 1.
Germline mutations in human mismatch repair genes (hMSH2, hMSH6, hMLH1, and hPMS2) are responsible for the majority of hereditary non-polyposis colorectal carcinoma (HNPCC). CpG dinucleotides in the hMSH2 and hMLH1 genes serve as hotspots for HNPCC mutations. These mutations lead to a deficiency in mismatch repair, resulting in a mutator phenotype where replication errors go unrepaired. Microsatellites, which are simple repetitive sequences, are particularly susceptible to such replication errors, and instability in these microsatellites is associated with the occurrence of HNPCC. The hMSH2 protein forms a heterodimeric complex with another MutS homolog protein, GTBP, called hMutS beta, which binds to insertion/deletion loops in DNA..
MSH6, a rabbit monoclonal antibody (RMab) for immunohistochemistry, is encoded by the mutS homolog 6 (MSH6) gene. This gene is notably associated with Hereditary Non-Polyposis Colorectal Cancer (HNPCC), an autosomal dominant condition that significantly increases cancer susceptibility. HNPCC is characterized by a familial tendency toward early onset colorectal carcinoma and a heightened risk for cancers in the gastrointestinal, urological, and female reproductive systems. It is recognized as the most prevalent form of inherited colorectal cancer in the Western world. MSH6 functions as a mismatch repair gene, which is often deficient in patients exhibiting high levels of microsatellite instability (MSI-H). The anti-MSH6 antibody is instrumental in screening patients and families for HNPCC. Notably, colon cancers with microsatellite instability typically have a better prognosis compared to those that are microsatellite-stable..
Secreted epithelial mucins are large macromolecules which exhibit extreme polydispersity. MUC-2 is the major intestinal mucin. O-glycans are attached to MUC-2 in a potentially diverse arrangement, which is crucial for their interaction with endogenous and exogenous lectins
Mucin 1, also known as MUC1, is a member of the mucin family and encodes a membrane-bound, glycosylated phosphoprotein. The protein is anchored to the apical surface of many epithelia by a transmembrane domain, the degree of glycosylation varying with cell type. Mucins are high molecular-weight glycoproteins which constitute the major component of the mucus layer that protects the gastric epithelium from chemical and mechanical aggressions.
The MUC1 protein serves a protective function by binding to pathogens and also functions in a cell-signaling capacity. Overexpression, aberrant intracellular localization, and changes in glycosylation of this protein have been associated with carcinomas. Multiple alternatively-spliced transcript variants that encode different isoforms of this gene have been reported, but the full-length nature of only some has been determined.
Mucin 1 (MUC1), also known as polymorphic epithelial mucin (PEM), is a transmembrane glycoprotein encoded by the MUC1 gene in humans. It plays a critical role in epithelial defense by interacting with and sequestering pathogens at the cell surface. Additionally, MUC1 is involved in intracellular signal transduction, contributing to the regulation of various cellular processes such as proliferation, differentiation, and immune responses
The major constituents of mucus, the viscous secretion that covers epithelial surfaces such as those in the trachea, colon, and cervix, are highly glycosylated proteins called mucins. These glycoproteins play important roles in the protection of the epithelial cells and have been implicated in epithelial renewal and differentiation. This gene encodes an integral membrane glycoprotein found on the cell surface, although secreted isoforms may exist.
MUC-4 transcripts have been detected in normal respiratory epithelium and lung. MUC-4 is a very specific (100%) and sensitive (90%) marker of lung adenocarcinomas and is negative for mesotheliomas. Reportedly, MUC-4 expression in invasive ductal carcinoma of the pancreas is an independent factor for poor prognosis.
MUC4 (mucin 4) is a high-molecular-weight, membrane-bound glycoprotein belonging to the mucin family, primarily expressed by epithelial cells in multiple normal tissues, including the lung, bronchus, stomach, colon, and cervix. In contrast, MUC4 expression is typically absent in normal pancreatic tissue but is markedly upregulated in the majority of pancreatic neoplasms, particularly pancreatic ductal adenocarcinoma. Furthermore, aberrant or elevated MUC4 expression has been documented in a range of epithelial malignancies, including gastric, colonic, and pulmonary adenocarcinomas. This differential expression profile highlights its potential diagnostic and prognostic utility in epithelial-derived tumors.
Mucin 5AC, also known as MUC5AC, is a human gene. The Mucin 5AC antigen is found in columnar mucous cells of surface gastric epithelium and in goblet cells of the fetal and precancerous colon but not in normal colon cells. Mucin genes are expressed in a regulated cell- and tissue-specific manner. MUC1 is detected in mucous cells of the surface epithelium and neck region of the gastric antrum, as well as in pyloric glands and oxyntic glands of the body region. MUC5AC is highly expressed in foveolar epithelium of both body and antrum, whereas MUC6 protein expression is limited to mucous neck cells of the body and pyloric glands of the antrum.
The mucin expression pattern of Gastric Carcinoma is heterogeneous. It includes mucins normally expressed in gastric mucosa (MUC1, MUC5AC and MUC6) and de novo expression of the intestinal mucin MUC2.The heterogeneous pattern of mucin expression, including the expression of the intestinal mucin MUC2, may provide new insights into the differentiation pathways of Gastric Carcinoma. It has been shown that in Gastric Carcinomas evaluated for expression of several mucins (MUC1, MUC2, MUC5AC and MUC6), mucin expression is associated with tumor type (MUC5AC with Diffuse and Infiltrative Carcinomas and MUC2 with Mucinous Carcinomas) but not with the clinico-biological behavior of the tumors. Mucin expression is associated with tumor location (MUC5AC with Antrum Carcinomas and MUC2 with Cardia Carcinomas), indirectly reflecting differences in tumor differentiation according to tumor location
This MAb recognizes the peptide core of gastric mucin M1 (recently identified as Mucin 5AC). Its epitope is located in the C-terminal cysteine rich part of the peptide core of MUC5AC. Its epitope is destroyed by beta-mercaptoethanol but not by periodate treatment. This mucin is present in primary ovarian mucinous cancer but usually absent in colorectal adenocarcinoma, thus showing an expression pattern opposite to MUC2. Together with a panel of antibodies, Anti-MUC5AC may be useful for differential identification of primary mucinous ovarian tumors from colon adenocarcinoma metastatic to the ovary. MUC5AC antibodies may also be useful for identification of intestinal metaplasia as well as in the identification of pancreatic carcinoma and pre-cancerous changes vs. normal pancreas
Mucin 6 (MUC6) is a human gene encoding a high-molecular-weight (~1,000 kDa) glycoprotein predominantly expressed by mucous cells of the gastric epithelium. Its expression is also observed in goblet cells of the fetal, precancerous, and neoplastic colon, but is absent in the normal adult colon. Beyond the gastrointestinal tract, MUC6 is expressed in additional epithelial tissues derived from the foregut, including epigastric and bronchial epithelia, as well as in M?llerian-derived structures such as the mucous cells of the endocervix and the urethral epithelium adjacent to the prostatic utriculus.
Antibodies directed against MUC6 demonstrate reliable reactivity with ethanol-fixed cultured epithelial cells, as well as ethanol- or formalin-fixed, paraffin-embedded tissue sections. Immunostaining highlights the surface epithelium of the normal gastric mucosa and shows positive reactivity in fetal, precancerous, and neoplastic colonic mucosa, whereas no staining is observed in normal adult colonic tissue.
Mucins are high molecular weight glycoproteins composed predominantly (approximately 80%) of carbohydrate moieties, with the remaining 20% consisting of a proteinaceous core. Gastric-type mucins are normally expressed in the human gastrointestinal epithelium. During colonic carcinogenesis, the reappearance of gastric mucin immunoreactivity is attributed to the re-expression of the peptide backbone characteristic of gastric or fetal-type colonic mucins.
MUM1 is one of the nuclear transcription factors necessary for development and activation of B lymphocytes. MUM1 belongs to the IRF gene family containing at least 10 widely expressed genes with similar DNA binding motif all involved in regulation of cell growth, transformation and induction of apoptosis as well as development of T-cell immune response.
The synonym of MUM1 is Interferon Regulatory Factor 4 (IRF4). MUM1 is found mainly in B-cell lymphoma and melanocytic lesions. Significant variation in positivity mainly due to chromosomal translocations involving MUM1 gene among T-cell lymphomas is observed. MUM1 is useful in a panel with other markers for subclassification of malignant lymphomas and identification of plasma cell differentiation.
Particularly MUM1 may be useful for the identification of plasma cell differentiation when morphologic evidence is lacking and Ig light chains are difficult to interpret
MUM1 is one of nuclear transcription factors necessary for development and activation of B lymphocytes. MUM1 belongs to the IRF gene family containing at least 10 widely expressed genes with similar DNA binding motif all involved in regulation of cell growth, transformation and induction of apoptosis as well as development of T-cell immune response.
The synonym of MUM1 is Interferon Regulatory Factor 4 (IRF4). MUM1 is found mainly in B-cell lymphoma and melanocytic lesions. Significant variation in positivity mainly due to chromosomal translocations involving MUM1 gene among T-cell lymphomas is observed. MUM1 is useful in a panel with other markers for subclassification of malignant lymphomas and identification of plasma cell differentiation.
Particularly MUM1 may be useful for the identification of plasma cell differentiation when morphologic evidence is lacking and Ig light chains are difficult to interpret.
The MBP (myelin basic protein) gene encodes a key structural component of the myelin sheath in oligodendrocytes and Schwann cells. In addition to neural tissues, MBP-related transcripts are also expressed in the bone marrow and immune system. These transcripts arise from the extended Golli-MBP gene, which includes three upstream exons not present in the classical MBP transcript. Alternative promoter usage and splicing from the Golli and MBP transcription start sites generate two transcript families. The Golli-derived transcripts include the unique upstream exons spliced in-frame with one or more MBP exons, producing chimeric proteins with an N-terminal Golli domain and C-terminal MBP sequences. In contrast, transcripts derived solely from the MBP promoter include only classical MBP exons, encoding the well-characterized myelin basic proteins. The evolutionary conservation of this genomic structure suggests functional and regulatory significance, with the MBP gene integrated within the larger Golli transcriptional unit.
Myeloperoxidase (MPO) is a peroxidase enzyme most abundantly present in neutrophil granulocytes. It is a lysosomal protein stored in azurophilic granules of the neutrophil. MPO has a heme pigment, which causes its green color in secretions rich in neutrophils, such as pus and some forms of mucus. Historically, immunohistochemical staining for myeloperoxidase was used in the diagnosis of Acute Myeloid Leukemia to demonstrate that the leukemic cells were derived from the myeloid lineage. Myeloperoxidase staining is still important in the diagnosis of Extramedullary Leukemia or Chloroma. Myeloperoxidase antibody detects granulocytes and monocytes in blood and precursors of granulocytes in the bone marrow. This antibody can detect myeloid cell populations of the bone marrow as well as in other sites.
Myo D1 belongs to a family of proteins known as myogenic regulatory factors (MRFs) and has a key role in regulating muscle differentiation. These bHLH (basic helix loop helix) transcription factors act sequentially in myogenic differentiation. MyoD1 is expressed in activated satellite cells, but not in quiescent satellite cells. In development, MyoD1 commitsmesoderm cells to a skeletal lineage, and then regulates that process. Itmay also play a role in muscle repair.
Recognizes a phosphor-protein of 45kDa, identified as MyoD1. This Mab does not cross react with myogenin, Myf5, or Myf6. Antibody to MyoD1 labels the nuclei of myoblasts in developing muscle tissues. MyoD1 is not detected in normal adult tissue, but is highly expressed in the tumor cell nuclei of rhabdomyosarcomas.
Occasionally nuclear expression of MyoD1 is seen in ectomesenchymoma and a subset of Wilm's tumors. Weak cytoplasmic staining is observed in several non-muscle tissues, including glandular epithelium and also in rhabdomyosarcomas, neuroblastomas, Ewing's sarcomas and alveolar soft part sarcomas.
Myogenin is a transcription factor specifically active in muscle cells and plays a crucial role as a myogenic regulatory factor. It belongs to a family of myogenic regulatory genes, which also includes MyoD, myf5, and MRF4. These genes encode transcription factors essential for muscle development. The expression of myogenin is restricted to cells of skeletal muscle origin, making it a valuable marker for muscle lineage tumors, particularly showing strong expression in Alveolar Rhabdomyosarcomas. Anti-myogenin antibodies label the nuclei of myoblasts in developing muscle tissue and are expressed in the tumor cell nuclei of Rhabdomyosarcoma and some Leiomyosarcomas. Positive nuclear staining may also be observed in Wilm?s Tumor
Myogenic factors are transcription factors consisting of an amino acid-rich region and a helix-loop-helix (HLH) structure, which can promote muscle development and maintain muscle-specific gene expression by transactivation.
Myogenin, one of the myogenic regulatory factors, plays a key role in determining the commitment and differentiation of primitive mesenchymal cells into skeletal muscle. The expression of Myogenin is restricted to cells of skeletal muscle origin, but it is not detected in adult skeletal muscles. It is therefore considered to be an extremely reliable and specific marker for diagnosing rhabdomyosarcomas.
Myoglobin, an intracellular hemoprotein expressed in the heart and oxidative skeletal myofibres of vertebrates, binds molecular oxygen and may facilitate oxygen transport from erythrocytes to mitochondria, thereby maintaining cellular respiration during periods of high physiological demand. Anti-myoglobin labels skeletal and cardiac muscle cells. In combination with other striated muscle markers such as vimentin and myogenin, myoglobin is helpful in the identification of rhabdomyosarcoma and tumors with skeletal muscle differentiation. Recently, myoglobin has been reported to be expressed on epithelial cancer cells due to changed metabolic and environmental conditions. Myoglobin expression on cancer cells may play a causative role in tumor progression.
SMMS-1 is an antibody to smooth muscle myosin, a heavy chain that reacts with human visceral and vascular smooth muscle cells. The antibody also reacts with human myoepithelial cells.
It is very helpful in distinguishing between benign sclerosing breast lesions and infiltrating carcinomas in difficult cases since it strongly stains the myoepithelial layer in the benign lesions while it is negative in the infiltrating carcinomas